High Level Expression and Purification of King Cobra Cathelicidin OH-CATH30 in Escherichia coli as a Thioredoxin Fusion Protein

Tong Yi Sun

doi:10.4028/www.scientific.net/AMR.926-930.997

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High Level Expression and Purification of King Cobra Cathelicidin OH-CATH30 in Escherichia coli as a Thioredoxin Fusion Protein
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High Level Expression and Purification of King Cobra Cathelicidin OH-CATH30 in Escherichia coli as a Thioredoxin Fusion Protein

Abstract:

The Cathelicidin OH-CATH30 may have therapeutic potential against the systemic infections. However, it is a great challenge to obtain abundant OH-CATH30 by Escherichia coli expression system. The OH-CATH30 coding sequence was optimized and subcloned into vector pET-32a, allowing the peptide to be expressed as a thioredoxin fusion protein. The highest protein expression level obtained was 100 mg/L of bacterial culture. Before being cleaved with enterokinase, the released recombinant OH-CATH30 exhibited a in vitro strong antibacterial activity against the control strains.